1itz: Difference between revisions
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<StructureSection load='1itz' size='340' side='right'caption='[[1itz]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='1itz' size='340' side='right'caption='[[1itz]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1itz]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1itz]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ITZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ITZ FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1itz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1itz OCA], [https://pdbe.org/1itz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1itz RCSB], [https://www.ebi.ac.uk/pdbsum/1itz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1itz ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1itz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1itz OCA], [https://pdbe.org/1itz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1itz RCSB], [https://www.ebi.ac.uk/pdbsum/1itz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1itz ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/TKTC_MAIZE TKTC_MAIZE] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Transketolase|Transketolase]] | *[[Transketolase 3D structures|Transketolase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Zea mays]] | ||
[[Category: Bacher A]] | |||
[[Category: Bacher | [[Category: Bader G]] | ||
[[Category: Bader | [[Category: Busch M]] | ||
[[Category: Busch | [[Category: Echt S]] | ||
[[Category: Echt | [[Category: Fischer M]] | ||
[[Category: Fischer | [[Category: Freigang J]] | ||
[[Category: Freigang | [[Category: Gerhardt S]] | ||
[[Category: Gerhardt | [[Category: Huber R]] | ||
[[Category: Huber | |||
Latest revision as of 02:36, 28 December 2023
Maize Transketolase in complex with TPPMaize Transketolase in complex with TPP
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe gene specifying plastid transketolase (TK) of maize (Zea mays) was cloned from a cDNA library by southern blotting using a heterologous probe from sorghum (Sorghum bicolor). A recombinant fusion protein comprising thioredoxin of Escherichia coli and mature TK of maize was expressed at a high level in E. coli and cleaved with thrombin, affording plastid TK. The protein in complex with thiamine pyrophoshate was crystallized, and its structure was solved by molecular replacement. The enzyme is a C2 symmetric homodimer closely similar to the enzyme from yeast (Saccharomyces cerevisiae). Each subunit is folded into three domains. The two topologically equivalent active sites are located in the subunit interface region and resemble those of the yeast enzyme. Structure and properties of an engineered transketolase from maize.,Gerhardt S, Echt S, Busch M, Freigang J, Auerbach G, Bader G, Martin WF, Bacher A, Huber R, Fischer M Plant Physiol. 2003 Aug;132(4):1941-9. PMID:12913150[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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